The conformational stability of alpha-crystallin is rather low: Calorimetric results

被引：29

作者：

Gesierich, U ^{[1
]}

Pfeil, W ^{[1
]}

机构：

[1] UNIV POTSDAM,MAX DELBRUCK CTR MOL MED,D-13125 BERLIN,GERMANY

来源：

FEBS LETTERS | 1996年 / 393卷 / 2-3期

关键词：

alpha-crystallin; heat shock protein; scanning calorimetry; conformational stability; non-productive folding form; HEAT-SHOCK PROTEINS; BOVINE LENS CRYSTALLINS; MOLECULAR CHAPERONE; THERMAL-STABILITY; SPECTROSCOPY; SUBUNIT;

D O I：

10.1016/0014-5793(96)00867-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The eye lens protein and chaperonin, alpha-crystallin, was studied by differential scanning microcalorimetry, spectroscopy and size exclusion chromatography. The thermal transition of alpha-crystallin proceeds at T-trs = 59.8 +/- 0.6 degrees C with an enthalpy change of Delta H = 336 +/- 9 kJ per mol subunit, Disagreement between previous Delta H values could be attributed to a side reaction that leads, depending on the scan rate, to the formation of a non-productive folding form, The conformational stability of alpha-crystallin is rather low (Delta G = 24 +/- 5 kJ/mol of subunit), The minimal cooperative unit of alpha-crystallin is the monomeric subunit.

引用

页码：151 / 154

页数：4

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